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Title: Analysis of the Mechanism of Inhibition of Human Matrix Metalloproteinase 7 (MMP-7) Activity by Green Tea Catechins
Authors: MIYAKE, Tomoko
YASUKAWA, Kiyoshi  kyouindb  KAKEN_id
INOUYE, Kuniyo
Author's alias: 井上, 國世
Keywords: calcium
fluorescence
green tea catechins
matrix metalloproteinase
matrix metalloproteinase (MMP)-7
Issue Date: Aug-2011
Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Journal title: Bioscience, Biotechnology, and Biochemistry
Volume: 75
Issue: 8
Start page: 1564
End page: 1569
Abstract: Green tea catechins inhibit human matrix metalloproteinase 7 (MMP-7) activity non-competitively, and the galloyl group is essential for potent inhibition (Oneda et al., J. Biochem., 133, 571–576 (2003)). In this study, we analyzed the mechanism of this inhibition. In the hydrolysis of (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2, the inhibitory effects of (−)-epigallocatechin-3-gallate (EGCG), (−)-gallocatechin-3-gallate (GCG), (−)-epicatechin-3-gallate (ECG), and (−)-catechin-3-gallate (CG) increased with increasing pH levels from 7.0 to 8.5. The inhibitory effects of EGCG and GCG were more potent than those of ECG and CG, and increased with increasing CaCl2 concentrations from 10 to 50 mM. The fluorescence of EGCG and GCG decreased with increasing CaCl2 concentrations and with the addition of MMP-7, while those of ECG and CG did not. Our results suggest that these differences result from that in the B ring, EGCG and GCG have phenol hydroxyl groups at the 3′, 4′, and 5′ positions, while ECG and CG have them at the 3′ and 4′ positions.
Rights: © 2011 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
URI: http://hdl.handle.net/2433/176989
DOI(Published Version): 10.1271/bbb.110257
Appears in Collections:Journal Articles

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